TITLE

Characterization of interactions between polyphenolic compounds and human serum proteins by capillary electrophoresis

AUTHOR(S)
Diniz, Andréa; Escuder-Gilabert, Laura; Lopes, Norbertor P.; Villanueva-Camañas, Rosa María; Sagrado, Salvador; Medina-Hernández, María José
PUB. DATE
May 2008
SOURCE
Analytical & Bioanalytical Chemistry;May2008, Vol. 391 Issue 2, p625
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The interaction of ten natural polyphenolic compounds (chlorogenic acid, apigenin, catechin, epicatechin, flavanone, flavone, quercetin, rutin, vicenin-2 and vitexin) with human serum albumin and mixtures of human serum albumin and α1-acid glycoprotein under near physiological conditions is studied by capillary electrophoresis–frontal analysis. Furthermore, the binding of these polyphenolic compounds to total plasmatic proteins is evaluated using ultrafiltration and capillary electrophoresis. In spite of the relatively small differences in the chemical structures of the compounds studied, large differences were observed in their binding behaviours to plasmatic proteins. The hydrophobicity, the presence/absence of some functional groups, steric hindrance and spatial arrangement seem to be key factors in the affinity of natural polyphenols towards plasmatic proteins.
ACCESSION #
31815247

 

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